3QAC
Structure of amaranth 11S proglobulin seed storage protein from Amaranthus hypochondriacus L.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-06-05 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 63 |
| Unit cell lengths | 94.077, 94.077, 74.670 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.468 - 2.275 |
| R-factor | 0.1906 |
| Rwork | 0.188 |
| R-free | 0.24910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2e9q |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.216 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.5_2)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.340 |
| High resolution limit [Å] | 2.275 | 2.300 |
| Rmerge | 0.077 | 0.465 |
| Number of reflections | 17067 | |
| <I/σ(I)> | 16.3 | 4.01 |
| Completeness [%] | 99.0 | 99.3 |
| Redundancy | 4.3 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.6 | 293 | 16% PEG3350, 200mM ammonium formate, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
